Values CatLog read from this paper
Structure and mechanism of a cysteine sulfinate desulfinase engineered on the aspartate aminotransferase scaffold
PMID 22138634doi:10.1016/j.bbapap.2011.10.016Open in Browse
The paper itself is not on this site: read it at the publisher. This page lists only the values CatLog read from it.
CatLog read 5 records (13 values) from this paper: aspartate aminotransferase (EcAspAT) from Escherichia coli.
Read from the paper by an AI model and checked against the paper by a second, separate AI run; code converted the units. Values are in CatLog's units; each record opens in Browse with the line the paper prints and the checks.
| Enzyme | Organism | Substrate | kcat (s⁻¹) | Km (mM) | kcat/Km (mM⁻¹ s⁻¹) | Conditions | Open record |
|---|---|---|---|---|---|---|---|
| aspartate aminotransferase (EcAspAT)variant I33Q/Y214Q/R280Y | Escherichia coli | L-aspartate | 0.13 | 3.1 | 0.042 | pH 7.5, 25 °C | Open record: aspartate aminotransferase (EcAspAT) variant I33Q/Y214Q/R280Y, L-aspartate |
| aspartate aminotransferase (EcAspAT)variant I33Q/Y214Q/R280Y | Escherichia coli | L-aspartatebeta-decarboxylation to l-alanine | 0.07 | — | — | pH 7.5, 25 °C | Open record: aspartate aminotransferase (EcAspAT) variant I33Q/Y214Q/R280Y, L-aspartate |
| aspartate aminotransferase (EcAspAT)variant I33Q/Y214Q/R280Y | Escherichia coli | L-cysteine sulfinate | 0.05 | 0.1 | 0.5 | pH 7.5, 25 °C | Open record: aspartate aminotransferase (EcAspAT) variant I33Q/Y214Q/R280Y, L-cysteine sulfinate |
| aspartate aminotransferase (EcAspAT)variant I33Q/Y214Q/R280Y | Escherichia coli | L-cysteine sulfinatedesulfination to l-alanine plus SO2 | 0.5 | 0.1 | 5 | pH 7.5, 25 °C | Open record: aspartate aminotransferase (EcAspAT) variant I33Q/Y214Q/R280Y, L-cysteine sulfinate |
| aspartate aminotransferase (EcAspAT)variant I33Q/Y214Q/R280Y | Escherichia coli | L-glutamate | 0.03 | 5.2 | 0.006 | pH 7.5, 25 °C | Open record: aspartate aminotransferase (EcAspAT) variant I33Q/Y214Q/R280Y, L-glutamate |